MOLECULAR DYNAMIC SIMULATION OF THE INTERACTION OF THE ADAPTER WITH THE GENETIC

适配器与遗传相互作用的分子动力学模拟

• 批准号: 7956083
• 负责人: MARIA G KURNIKOVA
• 金额: $ 0.08万
• 依托单位: CARNEGIE-MELLON UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2009
• 资助国家: 美国
• 起止时间: 2009-08-01 至 2010-07-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7956083
• 关键词: Biological; Biomedical Research; Characteristics; Computer Retrieval of Information on Scientific Projects Database; DNA Sequence Rearrangement; Family Study; Funding; Genetic; Glutamate Receptor; Grant; High Performance Computing; Hydrogen Bonding; Institution; Ion Channel Protein; Ions; Ligand Binding; Methodology; Muscle Rigidity; Post-Translational Protein Processing; Proteins; Research; Research Personnel; Resources; Shapes; Source; Structure; System; United States National Institutes of Health; flexibility; molecular dynamics; novel; protein structure

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Using Molecular Dynamics (MD) simulations, computational protein modifications, and a novel theoretical methodology that determines structural rigidity/flexibility, we will concentrate on studying the family of ionotropic glutamate receptors (iGluR) due to their medicinal and biological importance. Also, we will continue to investigate the ion channel proteins with known and unknown tertiary structure. We will correlate flexibility of the protein structure with its functional characteristics, such as ion permeation and selectivity in open channels, and conformational rearrangements in gating. We are planning to analyze stability, i.e. rates and dynamics of formation and breakage of hydrogen bonds and hydrophobic contacts in protein systems that differ by size, flexibility, and a shape of ligand-binding cavities.

这个子项目是许多研究子项目中利用 资源由NIH/NCRR资助的中心拨款提供。子项目和 调查员(PI)可能从NIH的另一个来源获得了主要资金， 并因此可以在其他清晰的条目中表示。列出的机构是 该中心不一定是调查人员的机构。 利用分子动力学(MD)模拟、计算蛋白质修饰和一种确定结构刚性/柔性的新的理论方法，我们将集中研究具有药用和生物学意义的离子型谷氨酸受体(IGluR)家族。此外，我们还将继续研究具有已知和未知三级结构的离子通道蛋白。我们将把蛋白质结构的灵活性与其功能特征联系起来，例如开放通道中的离子渗透和选择性，以及门控中的构象重排。我们正计划分析稳定性，即蛋白质系统中氢键和疏水接触的形成和断裂的速率和动力学，这些蛋白质系统的大小、灵活性和配体结合腔的形状都不同。